ID   GUC2F_HUMAN             Reviewed;        1108 AA.
AC   P51841; Q9UJF1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 2.
DT   12-AUG-2020, entry version 194.
DE   RecName: Full=Retinal guanylyl cyclase 2;
DE            Short=RETGC-2 {ECO:0000303|PubMed:7777544};
DE            EC=4.6.1.2 {ECO:0000269|PubMed:7777544};
DE   AltName: Full=Guanylate cyclase 2F, retinal {ECO:0000312|HGNC:HGNC:4691};
DE   AltName: Full=Guanylate cyclase F;
DE            Short=GC-F;
DE   AltName: Full=Rod outer segment membrane guanylate cyclase 2;
DE            Short=ROS-GC2;
DE   Flags: Precursor;
GN   Name=GUCY2F; Synonyms=GUC2F, RETGC2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLN-296, TISSUE SPECIFICITY, ACTIVITY
RP   REGULATION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Retina;
RX   PubMed=7777544; DOI=10.1073/pnas.92.12.5535;
RA   Lowe D.G., Dizhoor A.M., Liu K., Gu Q., Spencer M., Laura R., Lu L.,
RA   Hurley J.B.;
RT   "Cloning and expression of a second photoreceptor-specific membrane retina
RT   guanylyl cyclase (RetGC), RetGC-2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:5535-5539(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   VARIANT [LARGE SCALE ANALYSIS] PRO-10.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [4]
RP   VARIANTS [LARGE SCALE ANALYSIS] CYS-40; ASN-160; TRP-230; PRO-284; GLN-305;
RP   CYS-308; HIS-380; ARG-434; ASP-568; GLN-628; LEU-677; LYS-794; VAL-1010;
RP   ARG-1052 AND ASP-1055.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [5]
RP   VARIANT ASP-872.
RX   PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA   de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA   Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA   del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA   Veltman J.A., Vissers L.E.;
RT   "Diagnostic exome sequencing in persons with severe intellectual
RT   disability.";
RL   N. Engl. J. Med. 367:1921-1929(2012).
RN   [6]
RP   ACTIVITY REGULATION.
RX   PubMed=29515371; DOI=10.3389/fnmol.2018.00052;
RA   Wimberg H., Janssen-Bienhold U., Koch K.W.;
RT   "Control of the Nucleotide Cycle in Photoreceptor Cell Extracts by Retinal
RT   Degeneration Protein 3.";
RL   Front. Mol. Neurosci. 11:52-52(2018).
CC   -!- FUNCTION: Responsible for the synthesis of cyclic GMP (cGMP) in rods
CC       and cones of photoreceptors (PubMed:7777544). Plays an essential role
CC       in phototransduction, by mediating cGMP replenishment (By similarity).
CC       May also participate in the trafficking of membrane-asociated proteins
CC       to the photoreceptor outer segment membrane (By similarity).
CC       {ECO:0000250|UniProtKB:Q5SDA5, ECO:0000269|PubMed:7777544}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC         Evidence={ECO:0000269|PubMed:7777544};
CC   -!- ACTIVITY REGULATION: Activated by GUCA1B when free calcium ions
CC       concentration is low, and inhibited by GUCA1B when free calcium ions
CC       concentration is high (PubMed:15772651). Inhibited by RD3
CC       (PubMed:29515371). {ECO:0000269|PubMed:15772651,
CC       ECO:0000269|PubMed:29515371}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with RD3; promotes the
CC       exit of GUCY2F from the endoplasmic reticulum and its trafficking to
CC       the photoreceptor outer segments (By similarity).
CC       {ECO:0000250|UniProtKB:P51842, ECO:0000250|UniProtKB:Q5SDA5}.
CC   -!- SUBCELLULAR LOCATION: Photoreceptor outer segment membrane
CC       {ECO:0000250|UniProtKB:O02740}; Single-pass type I membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Retina. Localized exclusively in the outer nuclear
CC       layer and inner segments of the rod and cone photoreceptor cells.
CC       {ECO:0000269|PubMed:7777544}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- PTM: There are 9 conserved cysteine residues in sensory guanylate
CC       cyclases, 6 in the extracellular domain, which may be involved in
CC       intra- or interchain disulfide bonds.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00099}.
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DR   EMBL; L37378; AAA74451.1; -; mRNA.
DR   EMBL; AL031387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS14545.1; -.
DR   PIR; I59385; I59385.
DR   RefSeq; NP_001513.2; NM_001522.2.
DR   SMR; P51841; -.
DR   BioGRID; 109241; 2.
DR   IntAct; P51841; 2.
DR   MINT; P51841; -.
DR   STRING; 9606.ENSP00000218006; -.
DR   iPTMnet; P51841; -.
DR   PhosphoSitePlus; P51841; -.
DR   BioMuta; GUCY2F; -.
DR   DMDM; 311033391; -.
DR   jPOST; P51841; -.
DR   MassIVE; P51841; -.
DR   MaxQB; P51841; -.
DR   PaxDb; P51841; -.
DR   PeptideAtlas; P51841; -.
DR   PRIDE; P51841; -.
DR   ProteomicsDB; 56431; -.
DR   Antibodypedia; 29460; 98 antibodies.
DR   DNASU; 2986; -.
DR   Ensembl; ENST00000218006; ENSP00000218006; ENSG00000101890.
DR   GeneID; 2986; -.
DR   KEGG; hsa:2986; -.
DR   UCSC; uc065aqx.1; human.
DR   CTD; 2986; -.
DR   DisGeNET; 2986; -.
DR   EuPathDB; HostDB:ENSG00000101890.4; -.
DR   GeneCards; GUCY2F; -.
DR   HGNC; HGNC:4691; GUCY2F.
DR   HPA; ENSG00000101890; Tissue enriched (retina).
DR   MIM; 300041; gene.
DR   neXtProt; NX_P51841; -.
DR   OpenTargets; ENSG00000101890; -.
DR   PharmGKB; PA29071; -.
DR   eggNOG; KOG1023; Eukaryota.
DR   GeneTree; ENSGT00940000162146; -.
DR   HOGENOM; CLU_001072_1_0_1; -.
DR   InParanoid; P51841; -.
DR   KO; K12322; -.
DR   OMA; ICRGGID; -.
DR   OrthoDB; 229634at2759; -.
DR   PhylomeDB; P51841; -.
DR   TreeFam; TF106338; -.
DR   BRENDA; 4.6.1.2; 2681.
DR   PathwayCommons; P51841; -.
DR   Reactome; R-HSA-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR   BioGRID-ORCS; 2986; 3 hits in 522 CRISPR screens.
DR   ChiTaRS; GUCY2F; human.
DR   GenomeRNAi; 2986; -.
DR   Pharos; P51841; Tbio.
DR   PRO; PR:P51841; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; P51841; protein.
DR   Bgee; ENSG00000101890; Expressed in right uterine tube and 9 other tissues.
DR   Genevisible; P51841; HS.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0005640; C:nuclear outer membrane; TAS:ProtInc.
DR   GO; GO:0097381; C:photoreceptor disc membrane; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0120200; C:rod photoreceptor outer segment; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0016941; F:natriuretic peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central.
DR   GO; GO:0001653; F:peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019934; P:cGMP-mediated signaling; IEA:Ensembl.
DR   GO; GO:0050908; P:detection of light stimulus involved in visual perception; IEA:Ensembl.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR   GO; GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   Gene3D; 3.30.70.1230; -; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR033484; GUCY2F.
DR   InterPro; IPR011645; HNOB_dom_associated.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF349; PTHR11920:SF349; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   SUPFAM; SSF55073; SSF55073; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   Cell projection; cGMP biosynthesis; Disulfide bond; GTP-binding; Lyase;
KW   Membrane; Nucleotide-binding; Polymorphism; Reference proteome;
KW   Sensory transduction; Signal; Transmembrane; Transmembrane helix; Vision.
FT   SIGNAL          1..50
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..1108
FT                   /note="Retinal guanylyl cyclase 2"
FT                   /id="PRO_0000012386"
FT   TOPO_DOM        51..467
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        491..1108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          532..812
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          884..1014
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00099"
FT   DISULFID        104..132
FT                   /evidence="ECO:0000250"
FT   DISULFID        452
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   DISULFID        460
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   VARIANT         10
FT                   /note="R -> P (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs755991142)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036419"
FT   VARIANT         40
FT                   /note="S -> C (in dbSNP:rs34228145)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042233"
FT   VARIANT         160
FT                   /note="I -> N (in dbSNP:rs33971675)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042234"
FT   VARIANT         230
FT                   /note="R -> W (in dbSNP:rs33973457)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042235"
FT   VARIANT         284
FT                   /note="L -> P (in dbSNP:rs12008095)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_009136"
FT   VARIANT         296
FT                   /note="R -> Q (in dbSNP:rs502209)"
FT                   /evidence="ECO:0000269|PubMed:7777544"
FT                   /id="VAR_009137"
FT   VARIANT         305
FT                   /note="R -> Q (in dbSNP:rs55966326)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042236"
FT   VARIANT         308
FT                   /note="Y -> C (in dbSNP:rs16985750)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_030633"
FT   VARIANT         380
FT                   /note="Q -> H (in dbSNP:rs2272925)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_030634"
FT   VARIANT         434
FT                   /note="G -> R (in dbSNP:rs56293008)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042237"
FT   VARIANT         568
FT                   /note="G -> D (in a glioblastoma multiforme sample; somatic
FT                   mutation; dbSNP:rs779221554)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042238"
FT   VARIANT         628
FT                   /note="R -> Q (in dbSNP:rs7883913)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_030635"
FT   VARIANT         677
FT                   /note="V -> L (in dbSNP:rs35474112)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042239"
FT   VARIANT         794
FT                   /note="E -> K (in dbSNP:rs35726803)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042240"
FT   VARIANT         872
FT                   /note="G -> D (in dbSNP:rs148663380)"
FT                   /evidence="ECO:0000269|PubMed:23033978"
FT                   /id="VAR_069424"
FT   VARIANT         1010
FT                   /note="A -> V (in dbSNP:rs55735218)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042241"
FT   VARIANT         1052
FT                   /note="K -> R (in a lung adenocarcinoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042242"
FT   VARIANT         1055
FT                   /note="E -> D (in a lung squamous cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_042243"
SQ   SEQUENCE   1108 AA;  124850 MW;  B047BBF1A3C009F9 CRC64;
     MFLGLGRFSR LVLWFAAFRK LLGHHGLASA KFLWCLCLLS VMSLPQQVWT LPYKIGVVGP
     WACDSLFSKA LPEVAARLAI ERINRDPSFD LSYSFEYVIL NEDCQTSRAL SSFISHHQMA
     SGFIGPTNPG YCEAASLLGN SWDKGIFSWA CVNYELDNKI SYPTFSRTLP SPIRVLVTVM
     KYFQWAHAGV ISSDEDIWVH TANRVASALR SHGLPVGVVL TTGQDSQSMR KALQRIHQAD
     RIRIIIMCMH SALIGGETQM HLLECAHDLK MTDGTYVFVP YDALLYSLPY KHTPYRVLRN
     NPKLREAYDA VLTITVESQE KTFYQAFTEA AARGEIPEKL EFDQVSPLFG TIYNSIYFIA
     QAMNNAMKEN GQAGAASLVQ HSRNMQFHGF NQLMRTDSNG NGISEYVILD TNLKEWELHS
     TYTVDMEMEL LRFGGTPIHF PGGRPPRADA KCWFAEGKIC HGGIDPAFAM MVCLTLLIAL
     LSINGFAYFI RRRINKIQLI KGPNRILLTL EDVTFINPHF GSKRGSRASV SFQITSEVQS
     GRSPRLSFSS GSLTPATYEN SNIAIYEGDW VWLKKFSLGD FGDLKSIKSR ASDVFEMMKD
     LRHENINPLL GFFYDSGMFA IVTEFCSRGS LEDILTNQDV KLDWMFKSSL LLDLIKGMKY
     LHHREFVHGR LKSRNCVVDG RFVLKVTDYG FNDILEMLRL SEEESSMEEL LWTAPELLRA
     PRGSRLGSFA GDVYSFAIIM QEVMVRGTPF CMMDLPAQEI INRLKKPPPV YRPVVPPEHA
     PPECLQLMKQ CWAEAAEQRP TFDEIFNQFK TFNKGKKTNI IDSMLRMLEQ YSSNLEDLIR
     ERTEELEIEK QKTEKLLTQM LPPSVAESLK KGCTVEPEGF DLVTLYFSDI VGFTTISAMS
     EPIEVVDLLN DLYTLFDAII GSHDVYKVET IGDAYMVASG LPKRNGSRHA AEIANMSLDI
     LSSVGTFKMR HMPEVPVRIR IGLHSGPVVA GVVGLTMPRY CLFGDTVNTA SRMESTGLPY
     RIHVSLSTVT ILQNLSEGYE VELRGRTELK GKGTEETFWL IGKKGFMKPL PVPPPVDKDG
     QVGHGLQPVE IAAFQRRKAE RQLVRNKP
//